8PP7

human RYBP-PRC1 bound to mononucleosome

Summary for 8PP7

• Entry DOI: 10.2210/pdb8pp7/pdb
• EMDB information: 17797
• Descriptor: Polycomb complex protein BMI-1, E3 ubiquitin-protein ligase RING2, Histone H3 (Fragment), ... (9 entities in total)
• Functional Keywords: ncprc1 complex, nucleosome, h2a, histones, ring1b, bmi1, heterodimer, e3 ligase, k119, gene regulation
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 14
• Total formula weight: 413744.06

Authors

Ciapponi, M.,Benda, C.,Mueller, J. (deposition date: 2023-07-06, release date: 2024-03-27, Last modification date: 2024-07-31)

Primary citation

Ciapponi, M.,Karlukova, E.,Schkolziger, S.,Benda, C.,Muller, J.
Structural basis of the histone ubiquitination read-write mechanism of RYBP-PRC1.
Nat.Struct.Mol.Biol., 31:1023-1027, 2024

PubMed Abstract: Histone H2A monoubiquitination (H2Aub1) by the PRC1 subunit RING1B entails a positive feedback loop, mediated by the RING1B-interacting protein RYBP. We uncover that human RYBP-PRC1 binds unmodified nucleosomes via RING1B but H2Aub1-modified nucleosomes via RYBP. RYBP interactions with both ubiquitin and the nucleosome acidic patch create the high binding affinity that favors RYBP- over RING1B-directed PRC1 binding to H2Aub1-modified nucleosomes; this enables RING1B to monoubiquitinate H2A in neighboring unmodified nucleosomes.

PubMed: 38528151
DOI: 10.1038/s41594-024-01258-x

Experimental method

ELECTRON MICROSCOPY (2.91 Å)